
On boiling the egg, what structural changes are taking place in the egg white?
A.The color of the egg white changes from colorless to white
B.${2^\circ }$ and ${3^\circ }$ structures are destroyed but ${1^\circ }$ structure remains intact
C.${1^\circ }$ , ${2^\circ }$ and ${3^\circ }$ structures of egg are destroyed
D.A reversible change takes place which can be reversed by decreasing the temperature.
Answer
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Hint:In this question we will learn about the structural changes happening in a substance. We will be discussing denaturation. We will also be discussing the primary, secondary, tertiary structures in denaturation. We will mainly discuss the changes that happen to compound’s primary, secondary, tertiary structures after undergoing the denaturation.
Complete answer:
Denaturation includes the breaking of a large number of the feeble linkages, or bonds (e.g., hydrogen bonds), inside a protein particle that are responsible for the exceptionally ordered structure of the protein in its regular (local) state. Denatured proteins have a looser, more irregular structure; most are insoluble. Denaturation can be achieved in different manners—e.g., by warming, by treatment with antacid, corrosive, urea, or cleansers, and by vivacious shaking.
The coagulation of egg white on bubbling is a common example of denaturation. Because of denaturation, the secondary and tertiary structures are destroyed however the primary structure stays unblemished.
So, the correct answer is option B.
Note:
Primary structure is the amino acid sequence.
Secondary structure is local interactions between stretches of a polypeptide chain and incorporates $\alpha - helix$ and $\beta - creased$ sheet structures.
Tertiary structure is the generally speaking three-dimension collapsing driven to a great extent by interactions between R groups.
Complete answer:
Denaturation includes the breaking of a large number of the feeble linkages, or bonds (e.g., hydrogen bonds), inside a protein particle that are responsible for the exceptionally ordered structure of the protein in its regular (local) state. Denatured proteins have a looser, more irregular structure; most are insoluble. Denaturation can be achieved in different manners—e.g., by warming, by treatment with antacid, corrosive, urea, or cleansers, and by vivacious shaking.
The coagulation of egg white on bubbling is a common example of denaturation. Because of denaturation, the secondary and tertiary structures are destroyed however the primary structure stays unblemished.
So, the correct answer is option B.
Note:
Primary structure is the amino acid sequence.
Secondary structure is local interactions between stretches of a polypeptide chain and incorporates $\alpha - helix$ and $\beta - creased$ sheet structures.
Tertiary structure is the generally speaking three-dimension collapsing driven to a great extent by interactions between R groups.
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